Mouse CTSZ / CTSX / Cathepsin Z (His Tag) recombinant protein

Mouse CTSZ / CTSX / Cathepsin Z (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Cathepsin Z (CTSZ), also known as Cathepsin X or CATX, belongs to the C1 family of lysosomal cysteine proteases. Its gene structure and activity properties show several unique features that distinguish it clearly from other human cysteine proteases. It has a very short pro-region that shows no similarity to those of other cathepsins and a three-residue insertion motif that forms a characteristic ‘mini loop’. Cathepsin Z exhibits mono- and di-peptidase activity at its C-terminus, and in contrast to cathepsin B, it does not act as an endopeptidase. It is restricted to the cells of theimmune system, predominantly monocytes, macrophages and dendritic cells. Cathepsin Z is widely expressed in human tissues, suggesting that this enzyme could be involved in the normal intracellular protein degradation taking place in all cell types. It is capable to cleave regulatory motifs at C-terminus affecting the function of targeted molecules. Cathepsin X may regulate also the maturation of dendritic cells, a process, which is crucial in the initiation of adaptive immunity. Furthermore, higher levels of Cathepsin Z are also found in tumour and immune cells of prostate and gastric carcinomas and inmacrophages of gastric mucosa, especially after infection by Helicobacter pylori. Cathepsin Z is also ubiquitously distributed in cancer cell lines and in primary tumors from different sources, suggesting that this enzyme may participate in tumor progression.

Cathepsin Z, isoform CRA_b

AU019819; AI787083; CTSX; RP23-59M10.3; CATHEPSIN X; CATHEPSIN Z; D2WSU143E; FLJ17088; CTSZ

Q9WUU7

Ctsz; mCG_9962

Human Cells

A DNA sequence encoding the mouse CTSZ (NP_071720.1) precursor (Met 1-Val 306) was expressed with a polyhistidine tag at the C-terminus.

Mouse

The secreted recombinant mouse CTSD pro form consists of 295 amino acids and has a predicted molecular mass of 33.2 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmCTSD is approximately 38 kDa due to glycosylation.

> 95 % as determined by SDS-PAGE

Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPPGFSAFK(Dnp)-OH (R&D Systems, Catalog # ES005). The specific activity is >1,200 pmoles/min/μg.